PLH33_FORAG
ID PLH33_FORAG Reviewed; 377 AA.
AC T2KPL9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Unsaturated 3S-rhamnoglycuronyl hydrolase {ECO:0000305};
DE EC=3.2.1.- {ECO:0000250|UniProtKB:L7P9J4};
DE AltName: Full=Glycosyl hydrolase 105 family protein P33 {ECO:0000305};
DE Short=P33_GH105 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P33 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P33;
DE AltName: Full=Ulvan hydrolase;
DE AltName: Full=Unsaturated beta-glucuronyl hydrolase {ECO:0000303|Ref.2};
DE Short=UGL;
DE Flags: Precursor;
GN ORFNames=BN863_22220 {ECO:0000312|EMBL:CDF79934.1};
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP FUNCTION.
RX DOI=10.1016/j.algal.2017.09.025;
RA Salinas A., French C.E.;
RT "The enzymatic ulvan depolymerisation system from the alga-associated
RT marine flavobacterium Formosa agariphila.";
RL Algal Res. 27:335-344(2017).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: Unsaturated beta-glucuronyl hydrolase involved in ulvan
CC degradation (Ref.2, PubMed:31285597). Ulvan is the main polysaccharide
CC component of the Ulvales (green seaweed) cell wall. It is composed of
CC disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S)
CC linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose
CC (Xyl) (Probable). Unsaturated 3S-rhamnoglycuronyl hydrolase works
CC together with ulvan lyases to fully degrade the ulvan polymer,
CC catalyzing specifically the cleavage of the unsaturated 4-deoxy-L-
CC threo-hex-4-enopyranosiduronic acid (deltaUA) of deltaUA-Rha3S
CC disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides, the end
CC products of the ulvan lyase reaction. Also hydrolases deltaUA-Rha3S-
CC IduA-Rha3S and deltaUA-Rha3S-GlcA-Rha3S
CC tetrasaccharidestetrasaccharides. Prefers tetrasaccharides over
CC disaccharides and prefers an uronic residue at subsite +2 (By
CC similarity). {ECO:0000250|UniProtKB:L7P9J4,
CC ECO:0000269|PubMed:31285597, ECO:0000269|Ref.2, ECO:0000305|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 105 family.
CC {ECO:0000305}.
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DR EMBL; HG315671; CDF79934.1; -; Genomic_DNA.
DR RefSeq; WP_038530539.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KPL9; -.
DR SMR; T2KPL9; -.
DR STRING; 1347342.BN863_22220; -.
DR EnsemblBacteria; CDF79934; CDF79934; BN863_22220.
DR PATRIC; fig|1347342.6.peg.2229; -.
DR eggNOG; COG4225; Bacteria.
DR HOGENOM; CLU_042785_0_0_10; -.
DR OMA; NGSWHAS; -.
DR OrthoDB; 982403at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010905; Glyco_hydro_88.
DR Pfam; PF07470; Glyco_hydro_88; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..377
FT /note="Unsaturated 3S-rhamnoglycuronyl hydrolase"
FT /id="PRO_5004602909"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O34559"
SQ SEQUENCE 377 AA; 43457 MW; D8F7540C37ED35F9 CRC64;
MKNQALKILT LCVLVGSAMS LKLYAQKGLN HSEIEAKMIK ALEWQEAHPI FALAPTDWTE
GAYYIGVSRA HKTTQDMMYM AALKNQAYWN NWQTYSRLHH ADDVAISYSY IYIGMNDKRP
GFVNLEPTKK FLDAHLHEDD EWKAGTDKSA SGKTILWWWC DALFMAPPVL NLYAKHTNQP
KYRDEMHKYY METYNQLYDK EERLFARDMR FVWKGTEKDL KEPNDKKIFW SRGNGWVLGG
LALLLDDMPN DYKHRTFYEN LFKDMASRIL ELQPKDGLWR TSLLSPETYD HGEVSGSGFY
TFALAWGVNN GLLDRNKYEP AVKKAWKALA DCQHEDGRVG WVQNIGASPE PASADSWQNF
GTGAFLMAGS EVLKLEE
